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J. Biol. Chem., Vol. 280, Issue 38, 32729-32735, September 23, 2005

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Subunit Architecture of the Conserved Oligomeric Golgi Complex^*

Daniel Ungar1, Toshihiko Oka¶, Eliza Vasile, Monty Krieger, and Frederick M. Hughson2

From the Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544, the Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, and the ^¶Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka 812-8582, Japan

The conserved oligomeric Golgi (COG) complex is thought to function in intra-Golgi retrograde trafficking mediated by coat protein I vesicles, a pathway essential for the proper structure and function of the Golgi apparatus. Previous work suggested that COG might act as a tethering factor to mediate the initial attachment between coat protein I vesicles and Golgi membranes. Here, we present extensive in vitro co-translation and immunoprecipitation experiments leading to a new model for the overall architecture of the mammalian COG complex. The eight COG subunits (Cog1–8) are found to form two heterotrimeric subassemblies (Cog2/3/4 and Cog5/6/7) linked by a heterodimer composed of the remaining subunits (Cog1/8). This model is in excellent agreement with in vivo data presented in an accompanying paper (Oka, T., Vasile, E., Penman, M., Novina, C. D., Dykxhoorn, D. M., Ungar, D., Hughson, F. M., and Krieger, M. (2005) J. Biol. Chem. 280, 32736–32745).

Received for publication, April 26, 2005 , and in revised form, June 22, 2005.

^* This work was supported by a grant-in-aid (to F. M. H.) and a postdoctoral fellowship (to D. U.) from the American Heart Association (AHA) and by National Institutes of Health Grants GM071574 (to F. M. H.) and GM59115 (to M. K.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains a supplemental figure.

¹ New Jersey Board of Directors Fellow of the AHA.

² To whom correspondence should be addressed. Tel.: 609-258-4982; Fax: 609-258-6730; E-mail: hughson{at}princeton.edu.

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